www.nature.com/scientificreports
OPEN
Albumin adsorption on CoCrMo alloy surfaces Yu Yan, Hongjuan Yang, Yanjing Su & Lijie Qiao
received: 24 June 2015 accepted: 17 November 2015 Published: 17 December 2015
Proteins can adsorb on the surface of artificial joints immediately after being implanted. Although research studying protein adsorption on medical material surfaces has been carried out, the mechanism of the proteins’ adsorption which affects the corrosion behaviour of such materials still lacks in situ observation at the micro level. The adsorption of bovine serum albumin (BSA) on CoCrMo alloy surfaces was studied in situ by AFM and SKPFM as a function of pH and the charge of CoCrMo alloy surfaces. Results showed that when the specimens were uncharged, hydrophobic interaction could govern the process of the adsorption rather than electrostatic interaction, and BSA molecules tended to adsorb on the surfaces forming a monolayer in the side-on model. Results also showed that adsorbed BSA molecules could promote the corrosion process for CoCrMo alloys. When the surface was positively charged, the electrostatic interaction played a leading role in the adsorption process. The maximum adsorption occurred at the isoelectric point (pH 4.7) of BSA. The adsorption of proteins on solid surfaces has occupied a wide range of research projects due to its important role in biosensors, drug delivery systems, artificial tissues and so on1–4. For any foreign material transplanted into the body, the initial stage is the adsorption of proteins that would determine the subsequent performance of the transplant5. The adsorption of proteins on a solid surface is a complex process combing hydrophobic, electrostatic and hydrogen-bonding interactions. Recent studies consider whether the hydrophobic interaction or the electrostatic interaction is more important, depending on the properties of the solid surface and the surrounding environment3. There are abundant reports on the adsorption of various proteins on different material surfaces2–8. Adsorption is the process whereby molecules adhere to solid surfaces. Such proteins adsorption is an instantaneous process occurring on its first contact with biological fluids and tissues. Protein adsorption studies have focused on the adsorption kinetics, dynamics and thermodynamics, the spectroscopic studies of protein structure and function in the adsorbed state5,6. The nature and amount of the protein adsorption layer depends on materials surface properties, such as wettability, polar or ionic interaction, chemical structures and topography of the surface7. Proteins tend to unfold or denature on the surface of some materials due to the change of energy9. However, the denaturation of proteins on metal surface is still under investigation. The electrostatic interaction is related to both the charge of the solid surface and the pH value of the solution that determines the net charge of the proteins. In biological systems, the pH value is around 7.4 in normal conditions. However, some conditions such as infection and healing processes may alter the pH values around the implants9. Moreover, pH falls as a consequence of the hydrolysis of the metal ions released from artificial joints. Therefore, systematic studies of the influence of pH on protein adsorption are necessary. The techniques used most often to study the behaviour of protein adsorption on a solid surface include Raman Spectroscopy10, quartz crystal microbalance (QMC), ellipsometry, infrared spectroscopy and various electrochemical techniques11–13. Surface kelvin potential force microscopy (SKPFM) makes it possible to obtain the morphology and the corresponding surface potential at the same time. From the morphology images, the thickness and the distribution of the proteins can be obtained. In addition, SKPFM can provide insight into the interaction between proteins and the metal substrates at the micro level. SKPFM can also be used to explain the problems related to corrosion of the tested material covered with organic species. CoCrMo alloy is widely used as a biomaterial in dental skeletal structures and hip and knee joint replacements owing to its good biocompatibility and excellent mechanical behaviour14. Although there have been a few studies reporting the effect of proteins on the corrosion behaviours of biomedical materials, the mechanisms through which proteins influence the corrosion reactions are still not fully understood. The main objective of this work is to elucidate the effects of the pH and the surface charge on the adsorption of albumin on CoCrMo alloy surfaces Corrosion and Protection Center, Key Laboratory for Environmental Fracture (MOE) University of Science and Technology Beijing, Beijing 100083, China. Correspondence and requests for materials should be addressed to Y.Y. (email: [email protected])
Scientific Reports | 5:18403 | DOI: 10.1038/srep18403
1
www.nature.com/scientificreports/ Elements
Co
Mo
Cr
C
Ni
Si
Mn
Content
62.45
5.43
28.32
0.20
OPEN
Albumin adsorption on CoCrMo alloy surfaces Yu Yan, Hongjuan Yang, Yanjing Su & Lijie Qiao
received: 24 June 2015 accepted: 17 November 2015 Published: 17 December 2015
Proteins can adsorb on the surface of artificial joints immediately after being implanted. Although research studying protein adsorption on medical material surfaces has been carried out, the mechanism of the proteins’ adsorption which affects the corrosion behaviour of such materials still lacks in situ observation at the micro level. The adsorption of bovine serum albumin (BSA) on CoCrMo alloy surfaces was studied in situ by AFM and SKPFM as a function of pH and the charge of CoCrMo alloy surfaces. Results showed that when the specimens were uncharged, hydrophobic interaction could govern the process of the adsorption rather than electrostatic interaction, and BSA molecules tended to adsorb on the surfaces forming a monolayer in the side-on model. Results also showed that adsorbed BSA molecules could promote the corrosion process for CoCrMo alloys. When the surface was positively charged, the electrostatic interaction played a leading role in the adsorption process. The maximum adsorption occurred at the isoelectric point (pH 4.7) of BSA. The adsorption of proteins on solid surfaces has occupied a wide range of research projects due to its important role in biosensors, drug delivery systems, artificial tissues and so on1–4. For any foreign material transplanted into the body, the initial stage is the adsorption of proteins that would determine the subsequent performance of the transplant5. The adsorption of proteins on a solid surface is a complex process combing hydrophobic, electrostatic and hydrogen-bonding interactions. Recent studies consider whether the hydrophobic interaction or the electrostatic interaction is more important, depending on the properties of the solid surface and the surrounding environment3. There are abundant reports on the adsorption of various proteins on different material surfaces2–8. Adsorption is the process whereby molecules adhere to solid surfaces. Such proteins adsorption is an instantaneous process occurring on its first contact with biological fluids and tissues. Protein adsorption studies have focused on the adsorption kinetics, dynamics and thermodynamics, the spectroscopic studies of protein structure and function in the adsorbed state5,6. The nature and amount of the protein adsorption layer depends on materials surface properties, such as wettability, polar or ionic interaction, chemical structures and topography of the surface7. Proteins tend to unfold or denature on the surface of some materials due to the change of energy9. However, the denaturation of proteins on metal surface is still under investigation. The electrostatic interaction is related to both the charge of the solid surface and the pH value of the solution that determines the net charge of the proteins. In biological systems, the pH value is around 7.4 in normal conditions. However, some conditions such as infection and healing processes may alter the pH values around the implants9. Moreover, pH falls as a consequence of the hydrolysis of the metal ions released from artificial joints. Therefore, systematic studies of the influence of pH on protein adsorption are necessary. The techniques used most often to study the behaviour of protein adsorption on a solid surface include Raman Spectroscopy10, quartz crystal microbalance (QMC), ellipsometry, infrared spectroscopy and various electrochemical techniques11–13. Surface kelvin potential force microscopy (SKPFM) makes it possible to obtain the morphology and the corresponding surface potential at the same time. From the morphology images, the thickness and the distribution of the proteins can be obtained. In addition, SKPFM can provide insight into the interaction between proteins and the metal substrates at the micro level. SKPFM can also be used to explain the problems related to corrosion of the tested material covered with organic species. CoCrMo alloy is widely used as a biomaterial in dental skeletal structures and hip and knee joint replacements owing to its good biocompatibility and excellent mechanical behaviour14. Although there have been a few studies reporting the effect of proteins on the corrosion behaviours of biomedical materials, the mechanisms through which proteins influence the corrosion reactions are still not fully understood. The main objective of this work is to elucidate the effects of the pH and the surface charge on the adsorption of albumin on CoCrMo alloy surfaces Corrosion and Protection Center, Key Laboratory for Environmental Fracture (MOE) University of Science and Technology Beijing, Beijing 100083, China. Correspondence and requests for materials should be addressed to Y.Y. (email: [email protected])
Scientific Reports | 5:18403 | DOI: 10.1038/srep18403
1
www.nature.com/scientificreports/ Elements
Co
Mo
Cr
C
Ni
Si
Mn
Content
62.45
5.43
28.32
0.20
